Research workbench
Translocator domain of autotransporter nalp from neisseria meningitidis
Analyse Translocator domain of autotransporter nalp from neisseria meningitidis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UYN
- Type
- protein
- Length
- 279 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nalp
- UniProt
- Q8GKS5
- Ligands
- CXE, SO4
- Pockets
- 3 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 8% helix, 70% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Nalp | protein | 279 | 8% helix, 70% strand | Q8GKS5 |
Ligands and binding sites
- CXE · Pentaethylene glycol monodecyl ether · ligand · chains X
- SO4 · Sulfate ion · ion · 2 copies · chains X
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 425 | 0.80 | 0.88 | 66 | empty |
| 2 | 70 | 0.73 | 0.98 | 29 | empty |
| 3 | 207 | 0.58 | 0.80 | 32 | empty |
Compared structures
- 1UYN · Translocator domain of autotransporter NalP from Neisseria meningitidis · the same entry in another collection · chain X against X, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q8GKS5
- Elsewhere: RCSB PDB 1UYN · PDBe 1UYN · UniProt Q8GKS5
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.